Protein metalation by two structurally related gold(I) carbene complexes: An ESI MS study

Anticancer Diiron Vinyliminium Complexes: A Structure–Activity Relationship Study

“…Sample preparation. Cytochrome c (Cyt c) was commercially available and used as received; the TrxR dodecapeptide ( TrxR-pept ) was synthesized as reported in the literature [ 63 , 64 ]. The stock solutions of the selected iron-based complexes were prepared in DMSO up to a final concentration of 10 −2 M. The stock solution of TrxR-pept was prepared in LC-MS grade water by dissolving the required amount of lyophilized peptide to reach a final concentration of 10 −3 M. The stock solution of Cyt c 10 −3 M was prepared by dissolving the required amount of protein in 2 mM ammonium acetate solution at pH 6.8.…”

Mass spectrometry insights into interactions of selenoprotein P with auranofin and cisplatin

“…7 In studies of intact TrRx, the presence of multiple sites of interactions (other than SeCys) accessible to Au(I) has been suggested. 8 Peptide models of TrxR: 4-mer 9 and 11-mer peptides, 10,11 corresponding to the C-terminal SeCys-containing motif of human TrxR, were reacted with a panel of gold(I) complexes and the gold binding sites were identied as SeCys and Cys. In an attempt to study TrxR interaction with Pt-anticancer drugs, it was suggested that terpyridine-platinum(II) is bound to Cys in the GCCG motif of a TrxR mutant in which SeCys-498 was replaced by Cys (Lo et al 2009).…”

Synthesis, chemical characterization, and biological evaluation of a novel auranofin derivative as an anticancer agent

“…Two main signals are detected: one at 66 438 Da assigned to the native protein, and another at 66 558 Da due to cysteinylation of Cys34. 26,31 Upon addition of 3 equivalents of AFETT an almost complete metallation of the albumin is detected after 24h, as evidenced by an intense peak at 66 752 Da corresponding to the binding to HSA of the [Au(PEt 3 )] + fragment. Since gold(I) compounds are highly thiophilic, we might assume that the Cys34 residue could be a preferential binding site for the gold(I) fragments, as already demonstrated for auranofin.…”

“…This novel compound, namely ethylthiosalicylate (triethylphosphine) gold(I) (AFETT hereafter), has been characterized in detail from the chemical point of view and its structure solved through single-crystal X-ray diffraction. Its reactivity against representative biological molecular targets (such as HSA and the TrxR synthetic dodecapeptide) was assessed through 31 P NMR and ESI-MS experiments. Moreover, the antiproliferative effects of the new compound were tested on human ovarian and colorectal cancer cell lines, demonstrating its ability to induce cell apoptosis and the blockade of the cell cycle.…”